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Conserved domains on  [gi|1384865987|ref|NP_001349772|]
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histone acetyltransferase p300 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1280-1586 1.15e-97

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.


:

Pssm-ID: 400497  Cd Length: 348  Bit Score: 319.34  E-value: 1.15e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1280 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1359
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1360 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1434
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1435 KRLQEWYKKMLDKAVSE-------RIVHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1489
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1490 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGM 1547
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1384865987 1548 PNVSNDLSQKLYATMEKHkevFFVIRLIAGPAANSLPPI 1586
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1025-1132 2.61e-77

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


:

Pssm-ID: 99927  Cd Length: 108  Bit Score: 250.82  E-value: 2.61e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1025 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWL 1104
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                           90       100
                   ....*....|....*....|....*...
gi 1384865987 1105 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1132
Cdd:cd05495     81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 566-646 7.53e-48

KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun.


:

Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.74  E-value: 7.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  566 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 645
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80


                   .
gi 1384865987  646 E 646
Cdd:pfam02172   81 E 81
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 1966-2072 3.55e-35

Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery.


:

Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 130.73  E-value: 3.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1966 QPPWSQGGLPQPQQLQS--GMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GISPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2041
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQmqGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1384865987 2042 QQVLSILHANPQLLAAFIKQRAAKYANSNPQ 2072
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1144-1216 1.80e-32

atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


:

Pssm-ID: 276805  Cd Length: 73  Bit Score: 121.63  E-value: 1.80e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865987 1144 FSPQTLCCYGKqlCTIPRD--ATYYSYQ---NRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKNDTLDPE 1216
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1642-1682 2.72e-28

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


:

Pssm-ID: 239077  Cd Length: 41  Bit Score: 108.42  E-value: 2.72e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1384865987 1642 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1682
Cdd:cd02337      1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 347-414 5.16e-28

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 108.63  E-value: 5.16e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865987  347 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVC 414
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1709-1777 1.88e-23

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 95.92  E-value: 1.88e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1384865987 1709 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1777
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
 1217-1251 2.82e-20

PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.


:

Pssm-ID: 277116  Cd Length: 40  Bit Score: 85.68  E-value: 2.82e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1384865987 1217 LFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLK 1251
Cdd:cd15646      6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1958-2382 7.93e-12

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 70.81  E-value: 7.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1958 MGPTGMQQQPPWSQGGLPQPQQLQSGMPRPamMSVAQHGQPLNMAPqPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSS 2037
Cdd:pfam09606   53 MSKKAAQQQQPQGGQGNGGMGGGQQGMPDP--INALQNLAGQGTRP-QMMGPMGPGPGGPMGQQMGGPGTASNLLASLGR 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2038 PLQQQQVLSILHANPQLL-AAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPaMQNMNPMQAGVQR 2116
Cdd:pfam09606  130 PQMPMGGAGFPSQMSRVGrMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGP-MGGQMPPQMGVPG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2117 AGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQfrdilrRQQMMQQQQQQGAGPGIGPGManhnqfQQPQGVGyppq 2196
Cdd:pfam09606  209 MPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ------QQQPQQQGQQSQLGMGINQMQ------QMPQGVG---- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2197 qqqrmQHHMQQMQQGNMGQIGQLPQALGAEAGASLQ--AYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQS--------- 2265
Cdd:pfam09606  273 -----GGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQnnYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGqvvalggln 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2266 ---PHLQGQQIPNSLSNQVR-------SPQPVPSPRPQSQPPHSSpsprMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQ 2335
Cdd:pfam09606  348 hleTWNPGNFGGLGANPMQRgqpgmmsSPSPVPGQQVRQVTPNQF----MRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1384865987 2336 GHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQ 2382
Cdd:pfam09606  424 ALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQ 470
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 691-828 1.00e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 51.19  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  691 QMSM------AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQflpqtQFPSQGMNVTnIPLAPSSGQAP 764
Cdd:pfam09770  202 AMRAqakkpaQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQ-----QHPGQGHPVT-ILQRPQSPQPD 275

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987  765 VSQAQMSSSSCPVNSPIMPPGSQGSHI-HCPQLPQPALHQNSPSPVPSRTPTP----HHTPPSIGAQQP 828
Cdd:pfam09770  276 PAQPSIQPQAQQFHQQPPPVPVQPTQIlQNPNRLSAARVGYPQNPQPGVQPAPahqaHRQQGSFGRQAP 344
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 88-318 3.29e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 49.24  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987   88 GSSPNLNMGVG-GPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTsGPNQGPTQSTGMMNSPVNQPAMGMN 166
Cdd:pfam09606   93 GTRPQMMGPMGpGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRV-GRMQPGGQAGGMMQPSSGQPGSGTP 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  167 TGMNAGMNPGmlaagngqgimpnQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGM 246
Cdd:pfam09606  172 NQMGPNGGPG-------------QGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAP 238

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1384865987  247 MNNPNPygspyTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAmdKKAVPGGGMPNMGQQPAPQVQQPGLVTP 318
Cdd:pfam09606  239 NQVAMQ-----QQQPQQQGQQSQLGMGINQMQQMPQGVGGGA--GQGGPGQPMGPPGQQPGAMPNVMSIGDQ 303
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1280-1586 1.15e-97

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.


Pssm-ID: 400497  Cd Length: 348  Bit Score: 319.34  E-value: 1.15e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1280 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1359
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1360 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1434
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1435 KRLQEWYKKMLDKAVSE-------RIVHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1489
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1490 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGM 1547
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1384865987 1548 PNVSNDLSQKLYATMEKHkevFFVIRLIAGPAANSLPPI 1586
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1025-1132 2.61e-77

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 250.82  E-value: 2.61e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1025 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWL 1104
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                           90       100
                   ....*....|....*....|....*...
gi 1384865987 1105 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1132
Cdd:cd05495     81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 566-646 7.53e-48

KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun.


Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.74  E-value: 7.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  566 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 645
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80


                   .
gi 1384865987  646 E 646
Cdd:pfam02172   81 E 81
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 1966-2072 3.55e-35

Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery.


Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 130.73  E-value: 3.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1966 QPPWSQGGLPQPQQLQS--GMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GISPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2041
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQmqGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1384865987 2042 QQVLSILHANPQLLAAFIKQRAAKYANSNPQ 2072
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
BROMO smart00297
bromo domain;
1022-1130 6.52e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.01  E-value: 6.52e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  1022 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNN 1101
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 1384865987  1102 AWLYNRKTSRVYKYCSKLSEVFEQEIDPV 1130
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1144-1216 1.80e-32

atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


Pssm-ID: 276805  Cd Length: 73  Bit Score: 121.63  E-value: 1.80e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865987 1144 FSPQTLCCYGKqlCTIPRD--ATYYSYQ---NRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKNDTLDPE 1216
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1642-1682 2.72e-28

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 108.42  E-value: 2.72e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1384865987 1642 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1682
Cdd:cd02337      1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 347-414 5.16e-28

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 108.63  E-value: 5.16e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865987  347 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVC 414
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 1130-1169 1.65e-23

CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


Pssm-ID: 399179  Cd Length: 40  Bit Score: 94.69  E-value: 1.65e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1384865987 1130 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1169
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1709-1777 1.88e-23

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 95.92  E-value: 1.88e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1384865987 1709 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1777
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1703-1781 3.49e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.12  E-value: 3.49e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  1703 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1778
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76


                    ...
gi 1384865987  1779 FCL 1781
Cdd:smart00551   77 KCV 79
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
347-417 3.73e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.35  E-value: 3.73e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1384865987   347 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQSGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 417
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
 1217-1251 2.82e-20

PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.


Pssm-ID: 277116  Cd Length: 40  Bit Score: 85.68  E-value: 2.82e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1384865987 1217 LFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLK 1251
Cdd:cd15646      6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1042-1118 9.74e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 82.75  E-value: 9.74e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1384865987 1042 QDPESLPFRQPVDPqlLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSK 1118
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 972-1131 1.43e-16

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 84.09  E-value: 1.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  972 SESKVEDCKM---ESTETEERSTELKTEIKEEEDQP--STSATQSSPAPgqskkkifkPEELRQALMPTLEALYRQDPES 1046
Cdd:COG5076     96 PESLRFDEIVflaIESVTPESGLGSLLMAHLKTSVKkrKTPKIEDELLY---------ADNKAIAKFKKQLFLRDGRFLS 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1047 LPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQE 1126
Cdd:COG5076    167 SIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKL 244


                   ....*
gi 1384865987 1127 IDPVM 1131
Cdd:COG5076    245 IEEIP 249
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1638-1680 2.32e-16

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 74.78  E-value: 2.32e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1384865987  1638 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHKME 1680
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1638-1679 3.82e-15

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.36  E-value: 3.82e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1384865987 1638 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNTKN-HDHKM 1679
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQTHKgGNHQM 45
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
 2024-2066 6.72e-13

Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP.


Pssm-ID: 411021 [Multi-domain]  Cd Length: 43  Bit Score: 64.60  E-value: 6.72e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1384865987 2024 ALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKY 2066
Cdd:cd20910      1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1958-2382 7.93e-12

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 70.81  E-value: 7.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1958 MGPTGMQQQPPWSQGGLPQPQQLQSGMPRPamMSVAQHGQPLNMAPqPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSS 2037
Cdd:pfam09606   53 MSKKAAQQQQPQGGQGNGGMGGGQQGMPDP--INALQNLAGQGTRP-QMMGPMGPGPGGPMGQQMGGPGTASNLLASLGR 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2038 PLQQQQVLSILHANPQLL-AAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPaMQNMNPMQAGVQR 2116
Cdd:pfam09606  130 PQMPMGGAGFPSQMSRVGrMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGP-MGGQMPPQMGVPG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2117 AGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQfrdilrRQQMMQQQQQQGAGPGIGPGManhnqfQQPQGVGyppq 2196
Cdd:pfam09606  209 MPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ------QQQPQQQGQQSQLGMGINQMQ------QMPQGVG---- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2197 qqqrmQHHMQQMQQGNMGQIGQLPQALGAEAGASLQ--AYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQS--------- 2265
Cdd:pfam09606  273 -----GGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQnnYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGqvvalggln 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2266 ---PHLQGQQIPNSLSNQVR-------SPQPVPSPRPQSQPPHSSpsprMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQ 2335
Cdd:pfam09606  348 hleTWNPGNFGGLGANPMQRgqpgmmsSPSPVPGQQVRQVTPNQF----MRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1384865987 2336 GHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQ 2382
Cdd:pfam09606  424 ALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQ 470
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 691-828 1.00e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 51.19  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  691 QMSM------AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQflpqtQFPSQGMNVTnIPLAPSSGQAP 764
Cdd:pfam09770  202 AMRAqakkpaQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQ-----QHPGQGHPVT-ILQRPQSPQPD 275

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987  765 VSQAQMSSSSCPVNSPIMPPGSQGSHI-HCPQLPQPALHQNSPSPVPSRTPTP----HHTPPSIGAQQP 828
Cdd:pfam09770  276 PAQPSIQPQAQQFHQQPPPVPVQPTQIlQNPNRLSAARVGYPQNPQPGVQPAPahqaHRQQGSFGRQAP 344
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 88-318 3.29e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 49.24  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987   88 GSSPNLNMGVG-GPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTsGPNQGPTQSTGMMNSPVNQPAMGMN 166
Cdd:pfam09606   93 GTRPQMMGPMGpGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRV-GRMQPGGQAGGMMQPSSGQPGSGTP 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  167 TGMNAGMNPGmlaagngqgimpnQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGM 246
Cdd:pfam09606  172 NQMGPNGGPG-------------QGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAP 238

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1384865987  247 MNNPNPygspyTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAmdKKAVPGGGMPNMGQQPAPQVQQPGLVTP 318
Cdd:pfam09606  239 NQVAMQ-----QQQPQQQGQQSQLGMGINQMQQMPQGVGGGA--GQGGPGQPMGPPGQQPGAMPNVMSIGDQ 303
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 646-787 1.79e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 46.72  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  646 EKRRTRLQKQNMLPNAAGMVPVSMNP-GPNMGQPQPGMTSSLNQFGQMSMAQPPIVPRQTPplQHHGQLAQPGAL--NPP 722
Cdd:TIGR01628  365 EQRRAHLQDQFMQLQPRMRQLPMGSPmGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTP--MGPGGPLRPNGLapMNA 442

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1384865987  723 MGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSpiMPPGSQ 787
Cdd:TIGR01628  443 VRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLAS--ATPQMQ 505
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 2217-2326 6.07e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2217 GQLPQALGAEAGASLQAYQQRLL----QQQMGSPVQPNPmSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprp 2292
Cdd:PRK10263   748 IVEPVQQPQQPVAPQQQYQQPQQpvapQPQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP------ 820

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1384865987 2293 qsQPPHSSPSPRMQPQPSPHHvSPQTSSPHPGLV 2326
Cdd:PRK10263   821 --QQPVAPQPQYQQPQQPVAP-QPQDTLLHPLLM 851
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1280-1586 1.15e-97

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.


Pssm-ID: 400497  Cd Length: 348  Bit Score: 319.34  E-value: 1.15e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1280 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1359
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1360 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1434
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1435 KRLQEWYKKMLDKAVSE-------RIVHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1489
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1490 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGM 1547
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1384865987 1548 PNVSNDLSQKLYATMEKHkevFFVIRLIAGPAANSLPPI 1586
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1025-1132 2.61e-77

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 250.82  E-value: 2.61e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1025 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWL 1104
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                           90       100
                   ....*....|....*....|....*...
gi 1384865987 1105 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1132
Cdd:cd05495     81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 566-646 7.53e-48

KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun.


Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.74  E-value: 7.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  566 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 645
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80


                   .
gi 1384865987  646 E 646
Cdd:pfam02172   81 E 81
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 1966-2072 3.55e-35

Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery.


Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 130.73  E-value: 3.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1966 QPPWSQGGLPQPQQLQS--GMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GISPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2041
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQmqGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1384865987 2042 QQVLSILHANPQLLAAFIKQRAAKYANSNPQ 2072
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
BROMO smart00297
bromo domain;
1022-1130 6.52e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.01  E-value: 6.52e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  1022 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNN 1101
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 1384865987  1102 AWLYNRKTSRVYKYCSKLSEVFEQEIDPV 1130
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1144-1216 1.80e-32

atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


Pssm-ID: 276805  Cd Length: 73  Bit Score: 121.63  E-value: 1.80e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865987 1144 FSPQTLCCYGKqlCTIPRD--ATYYSYQ---NRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKNDTLDPE 1216
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 1028-1127 1.09e-30

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 117.47  E-value: 1.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1028 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYN 1106
Cdd:cd04369      1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78

                           90       100
                   ....*....|....*....|.
gi 1384865987 1107 RKTSRVYKYCSKLSEVFEQEI 1127
Cdd:cd04369     79 GPGSPIYKDAKKLEKLFEKLL 99
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 1048-1125 2.36e-29

Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99930  Cd Length: 102  Bit Score: 113.53  E-value: 2.36e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865987 1048 PFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1125
Cdd:cd05498     23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1642-1682 2.72e-28

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 108.42  E-value: 2.72e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1384865987 1642 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1682
Cdd:cd02337      1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 347-414 5.16e-28

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 108.63  E-value: 5.16e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865987  347 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVC 414
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 1027-1127 7.83e-27

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 106.48  E-value: 7.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1027 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYN 1106
Cdd:cd05509      1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77

                           90       100
                   ....*....|....*....|.
gi 1384865987 1107 RKTSRVYKYCSKLSEVFEQEI 1127
Cdd:cd05509     78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 1041-1124 1.10e-25

Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99938  Cd Length: 99  Bit Score: 103.18  E-value: 1.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1041 RQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLS 1120
Cdd:cd05506     13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92


                   ....
gi 1384865987 1121 EVFE 1124
Cdd:cd05506     93 KIFE 96
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 1130-1169 1.65e-23

CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


Pssm-ID: 399179  Cd Length: 40  Bit Score: 94.69  E-value: 1.65e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1384865987 1130 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1169
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1709-1777 1.88e-23

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 95.92  E-value: 1.88e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1384865987 1709 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1777
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 1035-1127 2.51e-23

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99932  Cd Length: 103  Bit Score: 96.61  E-value: 2.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1035 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYK 1114
Cdd:cd05500     12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90

                           90
                   ....*....|...
gi 1384865987 1115 YCSKLSEVFEQEI 1127
Cdd:cd05500     91 MGKRLQAAFEKHL 103
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1703-1781 3.49e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.12  E-value: 3.49e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  1703 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1778
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76


                    ...
gi 1384865987  1779 FCL 1781
Cdd:smart00551   77 KCV 79
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 1030-1129 1.35e-22

Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99929  Cd Length: 107  Bit Score: 94.41  E-value: 1.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1030 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRK 1108
Cdd:cd05497      7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85

                           90       100
                   ....*....|....*....|.
gi 1384865987 1109 TSRVYKYCSKLSEVFEQEIDP 1129
Cdd:cd05497     86 GDDVVLMAQTLEKLFLQKLAQ 106
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 1045-1133 4.63e-22

Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99928  Cd Length: 119  Bit Score: 93.68  E-value: 4.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1045 ESLPFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYN-RKTSRVYKYCSKLSEVF 1123
Cdd:cd05496     22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99

                           90
                   ....*....|
gi 1384865987 1124 EQEIDPVMQS 1133
Cdd:cd05496    100 EEHIKKIISD 109
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 1023-1125 1.50e-21

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 91.58  E-value: 1.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1023 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKSPMDLSTIKRKLD---TGQYQEPWQYVDDIWLMF 1099
Cdd:cd05502      1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75

                           90       100
                   ....*....|....*....|....*.
gi 1384865987 1100 NNAWLYNRKTSRVYKYCSKLSEVFEQ 1125
Cdd:cd05502     76 KNCYKFNEEDSEVAQAGKELELFFEE 101
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
347-417 3.73e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.35  E-value: 3.73e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1384865987   347 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQSGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 417
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 1048-1124 1.11e-20

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99931  Cd Length: 102  Bit Score: 88.88  E-value: 1.11e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1384865987 1048 PFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFE 1124
Cdd:cd05499     23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
 1217-1251 2.82e-20

PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.


Pssm-ID: 277116  Cd Length: 40  Bit Score: 85.68  E-value: 2.82e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1384865987 1217 LFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLK 1251
Cdd:cd15646      6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 1026-1126 9.68e-20

Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99936  Cd Length: 115  Bit Score: 86.68  E-value: 9.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1026 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMF 1099
Cdd:cd05504      4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81

                           90       100
                   ....*....|....*....|....*..
gi 1384865987 1100 NNAWLYNRKTSRVYKYCSKLSEVFEQE 1126
Cdd:cd05504     82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1042-1118 9.74e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 82.75  E-value: 9.74e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1384865987 1042 QDPESLPFRQPVDPqlLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSK 1118
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
 1218-1249 1.78e-17

PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300/CBP family includes two highly homologous histone acetyltransferases (HATs), CREB-binding protein (CBP) and p300. CBP is also known as KAT3A or CREBBP. It specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). p300, also termed as KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CBP. and is involved in E1A function in cell cycle progression and cellular differentiation. Both CBP and p300 are co-activator proteins that have been implicated in cell cycle regulation, apoptosis, embryonic development, cellular differentiation and cancer. They associate with a number of DNA-binding transcription activators as well as general transcription factors (GTFs), thus mediating recruitment of basal transcription machinery to the promoter. They contain a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.


Pssm-ID: 277032  Cd Length: 37  Bit Score: 77.69  E-value: 1.78e-17
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1384865987 1218 FVECTECGRKMHQICVLHHEIIWPAGFVCDGC 1249
Cdd:cd15557      6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 1026-1116 4.35e-17

Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 79.02  E-value: 4.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1026 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLY 1105
Cdd:cd05510      6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83

                           90
                   ....*....|.
gi 1384865987 1106 NRKTSRVYKYC 1116
Cdd:cd05510     84 NSDPSHPLRRH 94
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 972-1131 1.43e-16

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 84.09  E-value: 1.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  972 SESKVEDCKM---ESTETEERSTELKTEIKEEEDQP--STSATQSSPAPgqskkkifkPEELRQALMPTLEALYRQDPES 1046
Cdd:COG5076     96 PESLRFDEIVflaIESVTPESGLGSLLMAHLKTSVKkrKTPKIEDELLY---------ADNKAIAKFKKQLFLRDGRFLS 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1047 LPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQE 1126
Cdd:COG5076    167 SIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKL 244


                   ....*
gi 1384865987 1127 IDPVM 1131
Cdd:COG5076    245 IEEIP 249
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1638-1680 2.32e-16

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 74.78  E-value: 2.32e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1384865987  1638 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHKME 1680
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 1031-1121 7.13e-16

Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99944  Cd Length: 98  Bit Score: 75.13  E-value: 7.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1031 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTS 1110
Cdd:cd05512      5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81

                           90
                   ....*....|.
gi 1384865987 1111 RVYKYCSKLSE 1121
Cdd:cd05512     82 IFYRAAVRLRD 92
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 1044-1124 3.72e-15

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 73.18  E-value: 3.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1044 PESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVF 1123
Cdd:cd05503     16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFF 93


                   .
gi 1384865987 1124 E 1124
Cdd:cd05503     94 E 94
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1638-1679 3.82e-15

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.36  E-value: 3.82e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1384865987 1638 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNTKN-HDHKM 1679
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQTHKgGNHQM 45
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
 1218-1251 4.29e-15

PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CBP is also known as CREBBP, since it specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). It augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. CBP contains a cysteine-histidine rich region, a KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.


Pssm-ID: 277117  Cd Length: 40  Bit Score: 70.78  E-value: 4.29e-15
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1384865987 1218 FVECTECGRKMHQICVLHHEIIWPAGFVCDGCLK 1251
Cdd:cd15647      7 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 1042-1129 9.75e-15

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 72.39  E-value: 9.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1042 QDPESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYN------RKTSRvYKY 1115
Cdd:cd05528     17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93

                           90
                   ....*....|....*..
gi 1384865987 1116 CSKLSEV---FEQEIDP 1129
Cdd:cd05528     94 CELRDEVhamIEAELDP 110
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 1041-1126 2.28e-14

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 71.14  E-value: 2.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1041 RQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSR-------VY 1113
Cdd:cd05511     13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVytkkakeML 90

                           90
                   ....*....|...
gi 1384865987 1114 KYCSKLSEVFEQE 1126
Cdd:cd05511     91 ELAEELLAEREEK 103
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1642-1678 2.88e-14

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 68.62  E-value: 2.88e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1384865987 1642 YTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHK 1678
Cdd:cd02249      1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 1061-1114 6.40e-14

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 69.64  E-value: 6.40e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1384865987 1061 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYK 1114
Cdd:cd05515     37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 1061-1132 1.40e-13

Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 68.90  E-value: 1.40e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1384865987 1061 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1132
Cdd:cd05524     39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
 1029-1125 1.98e-13

Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99939  Cd Length: 104  Bit Score: 68.16  E-value: 1.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1029 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNR- 1107
Cdd:cd05507      5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSs 81

                           90       100
                   ....*....|....*....|..
gi 1384865987 1108 ----KTSRVYKYCSKLSEVFEQ 1125
Cdd:cd05507     82 dhdvYLMAVEMQREVMSQIQQL 103
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
 2024-2066 6.72e-13

Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP.


Pssm-ID: 411021 [Multi-domain]  Cd Length: 43  Bit Score: 64.60  E-value: 6.72e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1384865987 2024 ALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKY 2066
Cdd:cd20910      1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 1024-1123 2.16e-12

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 65.25  E-value: 2.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1024 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAW 1103
Cdd:cd05505      4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73

                           90       100
                   ....*....|....*....|
gi 1384865987 1104 LYNRKTSRVYKYCSKLSEVF 1123
Cdd:cd05505     74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
 1028-1119 6.80e-12

Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99945  Cd Length: 98  Bit Score: 63.58  E-value: 6.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1028 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNR 1107
Cdd:cd05513      2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78

                           90
                   ....*....|..
gi 1384865987 1108 KTSRVYKYCSKL 1119
Cdd:cd05513     79 PDTIYYKAAKKL 90
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1958-2382 7.93e-12

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 70.81  E-value: 7.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1958 MGPTGMQQQPPWSQGGLPQPQQLQSGMPRPamMSVAQHGQPLNMAPqPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSS 2037
Cdd:pfam09606   53 MSKKAAQQQQPQGGQGNGGMGGGQQGMPDP--INALQNLAGQGTRP-QMMGPMGPGPGGPMGQQMGGPGTASNLLASLGR 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2038 PLQQQQVLSILHANPQLL-AAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPaMQNMNPMQAGVQR 2116
Cdd:pfam09606  130 PQMPMGGAGFPSQMSRVGrMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGP-MGGQMPPQMGVPG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2117 AGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQfrdilrRQQMMQQQQQQGAGPGIGPGManhnqfQQPQGVGyppq 2196
Cdd:pfam09606  209 MPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ------QQQPQQQGQQSQLGMGINQMQ------QMPQGVG---- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2197 qqqrmQHHMQQMQQGNMGQIGQLPQALGAEAGASLQ--AYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQS--------- 2265
Cdd:pfam09606  273 -----GGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQnnYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGqvvalggln 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2266 ---PHLQGQQIPNSLSNQVR-------SPQPVPSPRPQSQPPHSSpsprMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQ 2335
Cdd:pfam09606  348 hleTWNPGNFGGLGANPMQRgqpgmmsSPSPVPGQQVRQVTPNQF----MRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1384865987 2336 GHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQ 2382
Cdd:pfam09606  424 ALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQ 470
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1027-1115 2.40e-11

Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99952  Cd Length: 106  Bit Score: 62.34  E-value: 2.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1027 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKSPMDLSTIKRKLDtgQYQEPWQYVDDIW 1096
Cdd:cd05521      1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71

                           90
                   ....*....|....*....
gi 1384865987 1097 LMFNNAWLYNRKTSRVYKY 1115
Cdd:cd05521     72 QIPWNARLYNTKGSVIYKY 90
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 1174-1249 6.91e-11

PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277086  Cd Length: 73  Bit Score: 60.06  E-value: 6.91e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987 1174 FCEKCFNEIQGESVSLGddpsqpQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAG---FVCDGC 1249
Cdd:cd15614      1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADEtaeYVCPLC 73
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1060-1128 1.38e-10

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 60.52  E-value: 1.38e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987 1060 IPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEID 1128
Cdd:cd05516     37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 1061-1119 1.49e-10

Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99951  Cd Length: 103  Bit Score: 60.05  E-value: 1.49e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987 1061 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKL 1119
Cdd:cd05520     37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 1028-1127 2.57e-10

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 59.28  E-value: 2.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1028 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNA 1102
Cdd:cd05519      1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78

                           90       100
                   ....*....|....*....|....*
gi 1384865987 1103 WLYNRKTSRVYKYCSKLSEVFEQEI 1127
Cdd:cd05519     79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1061-1119 3.71e-10

Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 59.18  E-value: 3.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987 1061 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKL 1119
Cdd:cd05522     38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLL 96
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 1050-1113 1.11e-09

Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 57.46  E-value: 1.11e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987 1050 RQPVD-----PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVY 1113
Cdd:cd05518     21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 1026-1127 1.67e-08

Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99958  Cd Length: 128  Bit Score: 55.04  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1026 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAW 1103
Cdd:cd05529     23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101

                           90       100
                   ....*....|....*....|....
gi 1384865987 1104 LYNRKTSRVYKYCSKLSEVFEQEI 1127
Cdd:cd05529    102 TFNEPNSEIAKKAKRLSDWLLRIL 125
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 1061-1125 4.36e-08

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 53.16  E-value: 4.36e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1384865987 1061 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1125
Cdd:cd05525     39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 1643-1682 5.93e-08

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 50.72  E-value: 5.93e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1384865987 1643 TCNECKHHVE-TRWHCTVCEDYDLCITCYNTKNH-DHKMEKL 1682
Cdd:cd02340      2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLKI 43
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1945-2311 8.44e-08

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 57.71  E-value: 8.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1945 PMTRGPSGHLEPGMGPTGmqqQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGisplKPGTVSQQA 2024
Cdd:pfam09606  101 PMGPGPGGPMGQQMGGPG---TASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSG----QPGSGTPNQ 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2025 LQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQgvhsNPAM 2104
Cdd:pfam09606  174 MGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQ----QQPQ 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2105 QNMNPMQAG-----VQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGM 2179
Cdd:pfam09606  250 QQGQQSQLGmginqMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQ 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2180 ANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQhml 2259
Cdd:pfam09606  330 MNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQG--- 406

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1384865987 2260 PNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqsqpPHSSPSPRMQPQPSP 2311
Cdd:pfam09606  407 PGSQPPQSHPGGMIPSPALIPSPSPQM----------SQQPAQQRTIGQDSP 448
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 1061-1125 3.95e-07

Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99948  Cd Length: 103  Bit Score: 50.52  E-value: 3.95e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1384865987 1061 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1125
Cdd:cd05517     37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 1060-1125 6.63e-07

Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99933  Cd Length: 102  Bit Score: 49.73  E-value: 6.63e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1384865987 1060 IPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVyKYCSKLSEVFEQ 1125
Cdd:cd05501     30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1644-1676 8.10e-07

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 47.45  E-value: 8.10e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1384865987 1644 CNECKHH--VETRWHCTVCEDYDLCITCYNTKNHD 1676
Cdd:cd02339      3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKHD 37
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
 1026-1083 6.64e-06

Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99926 [Multi-domain]  Cd Length: 114  Bit Score: 47.05  E-value: 6.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987 1026 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKSPMDLSTI-KRKLDTG 1083
Cdd:cd05494      3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 691-828 1.00e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 51.19  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  691 QMSM------AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQflpqtQFPSQGMNVTnIPLAPSSGQAP 764
Cdd:pfam09770  202 AMRAqakkpaQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQ-----QHPGQGHPVT-ILQRPQSPQPD 275

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384865987  765 VSQAQMSSSSCPVNSPIMPPGSQGSHI-HCPQLPQPALHQNSPSPVPSRTPTP----HHTPPSIGAQQP 828
Cdd:pfam09770  276 PAQPSIQPQAQQFHQQPPPVPVQPTQIlQNPNRLSAARVGYPQNPQPGVQPAPahqaHRQQGSFGRQAP 344
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 88-318 3.29e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 49.24  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987   88 GSSPNLNMGVG-GPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTsGPNQGPTQSTGMMNSPVNQPAMGMN 166
Cdd:pfam09606   93 GTRPQMMGPMGpGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRV-GRMQPGGQAGGMMQPSSGQPGSGTP 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  167 TGMNAGMNPGmlaagngqgimpnQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGM 246
Cdd:pfam09606  172 NQMGPNGGPG-------------QGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAP 238

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1384865987  247 MNNPNPygspyTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAmdKKAVPGGGMPNMGQQPAPQVQQPGLVTP 318
Cdd:pfam09606  239 NQVAMQ-----QQQPQQQGQQSQLGMGINQMQQMPQGVGGGA--GQGGPGQPMGPPGQQPGAMPNVMSIGDQ 303
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 1642-1681 3.45e-05

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 43.19  E-value: 3.45e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1384865987 1642 YTCNECKHH--VETRWHCTVC--EDYDLCITC-YNTKNH--DHKMEK 1681
Cdd:cd02341      1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1957-2145 5.01e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1957 GMGPTGMQQQPPWSQgglPQPQQLQSGMPRPAMMSV-----AQHGQPLNMAPQPGlGQVGISPLKPGTVSQQALQNllRT 2031
Cdd:pfam09770  164 GVAPKKAAAPAPAPQ---PAAQPASLPAPSRKMMSLeeveaAMRAQAKKPAQQPA-PAPAQPPAAPPAQQAQQQQQ--FP 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2032 LRSPSSPLQQQQVLSILHANPQLLAAFIKQRaakyansnPQPIPGQPGMPQGQPGLQP-PTMPGQQGVHSNPAMQNMN-- 2108
Cdd:pfam09770  238 PQIQQQQQPQQQPQQPQQHPGQGHPVTILQR--------PQSPQPDPAQPSIQPQAQQfHQQPPPVPVQPTQILQNPNrl 309

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1384865987 2109 ---------PMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQ-MNMN 2145
Cdd:pfam09770  310 saarvgypqNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQlAQLS 356
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
 1026-1127 7.22e-05

Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99940  Cd Length: 99  Bit Score: 43.91  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1026 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLY 1105
Cdd:cd05508      2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77

                           90       100
                   ....*....|....*....|..
gi 1384865987 1106 NRKTSRVYKYCSKLSEVFEQEI 1127
Cdd:cd05508     78 NGGDHKLTQAAKAIVKICEQEM 99
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 670-828 7.29e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.08  E-value: 7.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  670 NPGPNMGQPQPGMTSSLNQFGQMSMAQPPIVPRQTPPLQHHGQlAQPGALNPPMGYGPRMQ--------QPSNQGQFLPQ 741
Cdd:pfam09606  282 QPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA-AHQQQMNQSVGQGGQVValgglnhlETWNPGNFGGL 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  742 TQFPSQGMNVTNIPL-APSSGQAPVSQAQ---MSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPH 817
Cdd:pfam09606  361 GANPMQRGQPGMMSSpSPVPGQQVRQVTPnqfMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQ 440

                          170
                   ....*....|.
gi 1384865987  818 HTPPSIGAQQP 828
Cdd:pfam09606  441 RTIGQDSPGGS 451
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 646-787 1.79e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 46.72  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  646 EKRRTRLQKQNMLPNAAGMVPVSMNP-GPNMGQPQPGMTSSLNQFGQMSMAQPPIVPRQTPplQHHGQLAQPGAL--NPP 722
Cdd:TIGR01628  365 EQRRAHLQDQFMQLQPRMRQLPMGSPmGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTP--MGPGGPLRPNGLapMNA 442

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1384865987  723 MGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSpiMPPGSQ 787
Cdd:TIGR01628  443 VRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLAS--ATPQMQ 505
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1900-2064 4.02e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 45.80  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1900 VEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMApmgmnPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQ 1979
Cdd:pfam09770  199 VEAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQF-----PPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQ 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 1980 LQSGMPRPAMMSVAQHGQPLNMAPQP----------GLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQqqqvlsiLH 2049
Cdd:pfam09770  274 PDPAQPSIQPQAQQFHQQPPPVPVQPtqilqnpnrlSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAP-------II 346

                          170
                   ....*....|....*.
gi 1384865987 2050 ANPQLLAA-FIKQRAA 2064
Cdd:pfam09770  347 THPQQLAQlSEEEKAA 362
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1642-1670 5.08e-04

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 39.97  E-value: 5.08e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1384865987 1642 YTCNECKHHV--ETRWHCTVCEDYDLCITCY 1670
Cdd:cd02335      1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 1643-1679 2.50e-03

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 37.95  E-value: 2.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1384865987 1643 TCNECK--HHVETRWHCTVCEDYDLCITCY----NTKNHD--HKM 1679
Cdd:cd02345      2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNslHIM 46
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 1643-1680 3.08e-03

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 37.71  E-value: 3.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1384865987 1643 TCNECKHHVET--RWHCTVCEDYDLCITCYNTKN----H--DHKME 1680
Cdd:cd02338      2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGVtterHlfDHPMQ 47
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 1643-1678 4.49e-03

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 37.18  E-value: 4.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1384865987 1643 TCNECKHHV--ETRWHCTVCEDYDLCITCYNTKNHDHK 1678
Cdd:cd02344      2 TCDGCQMFPinGPRFKCRNCDDFDFCENCFKTRKHNTR 39
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 2217-2326 6.07e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987 2217 GQLPQALGAEAGASLQAYQQRLL----QQQMGSPVQPNPmSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprp 2292
Cdd:PRK10263   748 IVEPVQQPQQPVAPQQQYQQPQQpvapQPQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP------ 820

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1384865987 2293 qsQPPHSSPSPRMQPQPSPHHvSPQTSSPHPGLV 2326
Cdd:PRK10263   821 --QQPVAPQPQYQQPQQPVAP-QPQDTLLHPLLM 851
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 653-839 6.40e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 41.92  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  653 QKQNMLPNAAGMVPVSMNPGPN-----MGQPQPGMTSS-----LNQFGQMSMAQPPIVPRQTP--PLQHHGQlaQPGALN 720
Cdd:pfam09606  218 QMGQQAQANGGMNPQQMGGAPNqvamqQQQPQQQGQQSqlgmgINQMQQMPQGVGGGAGQGGPgqPMGPPGQ--QPGAMP 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865987  721 PPMGYGprmQQPSNQGQflpQTQFPSQGMNVTNIPLAPSSGQAPVSQA-QMSSSSCPVNSPIMPPGSQGSHIHCPQLPQP 799
Cdd:pfam09606  296 NVMSIG---DQNNYQQQ---QTRQQQQQQGGNHPAAHQQQMNQSVGQGgQVVALGGLNHLETWNPGNFGGLGANPMQRGQ 369

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1384865987  800 ALHQNSPSPVPSRT-------------PTPHHTPPSIGAQQPPATTIPAPVPT 839
Cdd:pfam09606  370 PGMMSSPSPVPGQQvrqvtpnqfmrqsPQPSVPSPQGPGSQPPQSHPGGMIPS 422
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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